Abstract
We previously described a dominant suppressor of the splicing defect conferred by an A→;C intron branchpoint mutation in S. cerevisiae. Suppression occurs by increasing the frequency with which the mutant branchpoint is utilized. We have now cloned the genomic region encoding the prp16-1 suppressor function and have demonstrated that PRP16 is essential for viability. A 1071 amino acid open reading frame contains sequence motifs characteristic of an NTP binding fold and further similarities to a superfamily of proteins that includes members with demonstrated RNA-dependent ATPase activity. A single nucleotide change necessary to confer the prp16-1 suppressor phenotype results in a Tyr→Asp substitution near the "A site" consensus for NTP binding proteins. We propose that PRP16 is an excellent candidate for mediating one of the many ATP-requiring steps of spliceosome assembly and that accuracy of branchpoint recognition may be coupled to ATP binding and/or hydrolysis.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 705-717 |
| Number of pages | 13 |
| Journal | Cell |
| Volume | 60 |
| Issue number | 5 |
| DOIs | |
| State | Published - Mar 9 1990 |
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ASJC Scopus subject areas
- Cell Biology
- Molecular Biology
Cite this
A putative ATP binding protein influences the fidelity of branchpoint recognition in yeast splicing. / Burgess, Sean; Couto, Joseph R.; Guthrie, Christine.
In: Cell, Vol. 60, No. 5, 09.03.1990, p. 705-717.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - A putative ATP binding protein influences the fidelity of branchpoint recognition in yeast splicing
AU - Burgess, Sean
AU - Couto, Joseph R.
AU - Guthrie, Christine
PY - 1990/3/9
Y1 - 1990/3/9
N2 - We previously described a dominant suppressor of the splicing defect conferred by an A→;C intron branchpoint mutation in S. cerevisiae. Suppression occurs by increasing the frequency with which the mutant branchpoint is utilized. We have now cloned the genomic region encoding the prp16-1 suppressor function and have demonstrated that PRP16 is essential for viability. A 1071 amino acid open reading frame contains sequence motifs characteristic of an NTP binding fold and further similarities to a superfamily of proteins that includes members with demonstrated RNA-dependent ATPase activity. A single nucleotide change necessary to confer the prp16-1 suppressor phenotype results in a Tyr→Asp substitution near the "A site" consensus for NTP binding proteins. We propose that PRP16 is an excellent candidate for mediating one of the many ATP-requiring steps of spliceosome assembly and that accuracy of branchpoint recognition may be coupled to ATP binding and/or hydrolysis.
AB - We previously described a dominant suppressor of the splicing defect conferred by an A→;C intron branchpoint mutation in S. cerevisiae. Suppression occurs by increasing the frequency with which the mutant branchpoint is utilized. We have now cloned the genomic region encoding the prp16-1 suppressor function and have demonstrated that PRP16 is essential for viability. A 1071 amino acid open reading frame contains sequence motifs characteristic of an NTP binding fold and further similarities to a superfamily of proteins that includes members with demonstrated RNA-dependent ATPase activity. A single nucleotide change necessary to confer the prp16-1 suppressor phenotype results in a Tyr→Asp substitution near the "A site" consensus for NTP binding proteins. We propose that PRP16 is an excellent candidate for mediating one of the many ATP-requiring steps of spliceosome assembly and that accuracy of branchpoint recognition may be coupled to ATP binding and/or hydrolysis.
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UR - http://www.scopus.com/inward/citedby.url?scp=0025233806&partnerID=8YFLogxK
U2 - 10.1016/0092-8674(90)90086-T
DO - 10.1016/0092-8674(90)90086-T
M3 - Article
C2 - 2138057
AN - SCOPUS:0025233806
VL - 60
SP - 705
EP - 717
JO - Cell
JF - Cell
SN - 0092-8674
IS - 5
ER -